scholarly journals Mapping of the genes controlling high-molecular-weight glutelin subunits of rye on the long arm of chromosome 1R

1984 ◽  
Vol 44 (2) ◽  
pp. 117-123 ◽  
Author(s):  
N. K. Singh ◽  
K. W. Shepherd
Keyword(s):  
Molecular Weight ◽  
High Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Translocation Line ◽  
Sds Page ◽  
Chromosome 1R

SUMMARYThe gene(s) controlling the high-molecular-weight glutelin subunits in rye (designated as Glu-Rl) was mapped with respect to the centromere using a 1RL-1DS wheat-rye translocation line and sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE). Analysis of 479 seeds from test-crosses between a 1R/1RL-1DS heterozygote and the cultivar India 115, revealed 14·6% aneuploid and 3·95% recombinant progeny. Excluding the aneuploids, this locus was calculated to be 4·65 ± 1·04 cM from the centromere on the long arm of chromosome 1R, which is comparable to the position of the homoeologous loci in wheat and barley.

scholarly journals Arterial basement-membrane-like material isolated and characterized from rabbit aortic myomedial cells in culture

1983 ◽  
Vol 211 (2) ◽  
pp. 397-404 ◽  
Author(s):  
L Heickendorff ◽  
T Ledet
Keyword(s):  
Molecular Weight ◽  
Basement Membrane ◽  
High Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Periodic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Type I

Arterial basement-membrane-like material was isolated from rabbit aortic myomedial cell cultures by sonication and differential centrifugation. Isolated basement-membrane-like material was shown to be free of both cellular and matrix contaminants, on the basis of determinations of DNA, RNA, cholesterol, phosphorus and (Na+ + K+)-activated ATPase, combined with electron microscopy. Amino acid analyses showed that arterial basement-membrane-like material was composed of predominantly non-collagenous amino acids. Evaluated by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis, reduced basement-membrane-like material comprised six major and about 30 minor components in the Mr range 10 000-600 000. One of the major peptides (Mr 225 000) was disulphide-linked. Periodic acid-Schiff staining of gels indicated that most high-molecular-weight components were glycoproteins. Two-dimensional gel electrophoresis resolved reduced basement-membrane-like material into more than 100 components, with pI from 5 to 7. The disulphide-linked Mr-225 000 peptide appeared heterogeneous, with pI of 5.6-6.0, and was considered to represent fibronectin. All major peptides were of non-collagenous nature, on the basis of their susceptibility to pepsin and resistance to collagenase. Purified myomedial basement-membrane-like material contained collagenous peptides, as indicated by the presence of hydroxyproline and hydroxylysine. Sodium dodecyl sulphate/polyacrylamide-gel electrophoresis of pepsin-treated and reduced basement-membrane-like material revealed five high-molecular-weight collagenous components appearing in the Mr range 105 000-375 000 relative to type I collagen standards.

Identifikasi Daging Tikus Pada Produk Baso Dengan Metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE)

2018 ◽  
Vol 26 (2) ◽  
pp. 058
Author(s):  
Anna P. Roswiem ◽  
Triayu Septiani
Keyword(s):  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page

<em>Bahan<strong> </strong>baku untuk membuat baso adalah daging hewan, pada umumnya dari daging sapi, ayam, ikan dan babi. Di beberapa daerah di Indonesia terjadi kasus baso tikus. Tujuan penelitian ini adalah menguji ada tidaknya kandungan daging tikus pada produk baso yang dijual di pasar Cempaka Putih-Kecamatan Kramat Jakarta Pusat dan di pedagang baso atau mie baso di sekitar kampus Universitas YARSI Jakarta. Daging adalah protein salah satu metode untuk mengidentifikasi protein adalah metode Sodium Dodecyl Sulphate Polyacrylamide Gel Electrophoresis (SDS-PAGE).<strong> </strong>Hasil penelitian menunjukkan bahwa dari 6 sampel baso terindikasi ada 2 sampel baso dengan nomor 1 dan 5 yang dibuat dari campuran daging sapi dan tikus; ada 1 sampel baso dengan nomor 6 yang terbuat dari daging tikus; dan 2 sampel baso dengan nomor 2 dan 3 yang terbuat dari campuran sapi  dan babi, dan hanya 1 sampel baso dengan nomor sampel 4 yang benar-benar terbuat dari daging sapi.</em>

PROFIL PROTEIN VAKSIN Aeromonas hydrophila DAN Streptococcus agalactiae HASIL INAKTIVASI DENGAN FORMALIN: DIUJI MENGGUNAKAN Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis

2014 ◽  
Vol 9 (3) ◽  
pp. 449
Author(s):  
Desy Sugiani ◽  
Angela Mariana Lusiastuti ◽  
Sukenda Sukenda ◽  
Enang Harris
Keyword(s):  
Streptococcus Agalactiae ◽  
Sodium Dodecyl Sulphate ◽  
Total Protein ◽  
Aeromonas Hydrophila ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Sds Page ◽  
Neutral Buffer Formalin

Vaksin bakterin dalam bentuk protein merupakan salah satu tipe vaksin yang telah banyak dikembangkan. Protein digunakan sebagai vaksin biasanya dibuat dengan teknik inaktivasi formalin-killed. Vaksin ini biasanya lebih mudah dibuat, lebih murah, lebih stabil, dan mampu disimpan dalam waktu lama. Akan tetapi masih sedikit informasi mengenai efek perlakuan tersebut terhadap profil protein. Pada penelitian ini, untuk mengevaluasi profil protein, dilakukan inaktivasi sediaan vaksin dari isolat bakteri Aeromonas hydrophila AHL0905-2 dan Streptococcus agalactiae N14G dengan menambahkan 0,5% formalin dan 3% neutral buffer formalin (NBF) ke dalam biakan plasebo bakterin dan diinkubasi selama 24 jam. Kualitas produk vaksin ditentukan berdasarkan uji karakterisasi protein menggunakan metode Bradford dan SDS-PAGE. Hasil uji menunjukkan bahwa sediaan vaksin A. hydrophila dan S. agalactiae yang diinaktivasi dengan 3% NBF memiliki profil protein lebih variatif dibandingkan dengan sediaan vaksin yang diinaktivasi dengan 0,5% formalin. Akan tetapi, inaktivasi vaksin A. hydrophila dan S. agalactiae dengan 3% NBF menghasilkan berat total protein yang lebih rendah jika dibandingkan dengan dengan sediaan vaksin yang diinaktivasi dengan 0,5% formalin.

scholarly journals Purification and characterization of subcomponent C1q of the first component of mouse complement

1981 ◽  
Vol 193 (2) ◽  
pp. 621-629 ◽  
Author(s):  
K Yonemasu ◽  
T Sasaki
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Active Form ◽  
Sodium Dodecyl ◽  
Exchange Chromatography ◽  
Polyacrylamide Gel ◽  
Molecular Weight Range ◽  
Covalently Linked

1. Mouse C1q, a subcomponent of the first component of complement, has been purified in a highly haemolytically active form by a combination of precipitation with EGTA, ion-exchange chromatography and gel filtration. Yields ranged from 3 to 5 mg/200 ml of serum, and the activity of final preparations was in the range of 2 × 10(13)-4 × 10(13) C1q effective molecules/mg. 2. The molecular weight of mouse C1q was 439 500 +/- 1586, as determined by polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate. 3. Mouse C1q was shown to be composed of non-covalently linked subunits, all being in the molecular-weight range 45 000-46 000, and three covalently linked chains each having a molecular weight of approx. 23 000 as determined on polyacrylamide-gel electrophoresis in the presence of sodium dodecyl sulphate by using non-covalently and covalently linked subunits of human C1q as markers with known molecular weights calculated theoretically previously [Porter & Reid (1978) Nature (London) 275, 699-704]. 4. Mouse C1q contained hydroxyproline, hydroxylysine, a high percentage of glycine and approx. 9% carbohydrate. The absorption coefficient and nitrogen content of C1q were also determined.

scholarly journals Anomalous migration of leghaemoglobin on sodium dodecyl sulphate/polyacrylamide-gel electrophoresis

1978 ◽  
Vol 169 (1) ◽  
pp. 251-253 ◽  
Author(s):  
P Lehtovaara
Keyword(s):  
Molecular Weight ◽  
Sodium Dodecyl Sulphate ◽  
Gel Electrophoresis ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Polyacrylamide Gel ◽  
Relative Mobility ◽  
Concomitant Decrease ◽  
Helical Content

The estimate of the molecular weight of leghaemoglobin by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis is about 20% too low. This is due to an anomalously high limiting relative mobility. Leghaemoglobin binds 1.4 g of sodium dodecyl sulphate/g of protein with a concomitant decrease in the helical content from 71-72% to 49-51%.

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